Overexpression of PRMT6 does not suppress HIV-1 Tat transactivation in cells naturally lacking PRMT6.

ABSTRACT:

Background

Protein arginine methyltransferase 6 (PRMT6) can methylate the HIV-1 Tat, Rev and nucleocapsid proteins in a manner that diminishes each of their functions in in vitro assays, and increases the stability of Tat in human cells. In this study, we explored the relationship between PRMT6 and HIV-1 Tat by determining the domains in each protein required for interaction.

Methods

Through domain mapping and immunoprecipitation experiments, we determined that both the amino and carboxyl termini of PRMT6, and the activation domain within Tat are essential for interaction. Mutation of the basic domain of Tat did not affect the ability of PRMT6 to interact with Tat.

Results

We next used the A549 human alveolar adenocarcinoma cell line, which naturally expresses undetec

SUBMITTER: Sivakumaran H 

PROVIDER: S-EPMC3695826 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature